We have developed an analysis of protein conformation by circular dichroism (CD) that makes it possible to determine the fraction of helix with accuracy and of beta-form and beta-turn with fair to good results. A working hypothesis that surfactants, be they anionic, cationic and nonionic, provide a proteinaceous environment that can induce ordered structure of peptide segments will be extensively tested on naturally occurring oligopeptides with and without disulfide bonds, large fragments of proteins and intact proteins. The surfactants will later be expanded to include phospholipids that can be solubilized in a co-surfactant solution containing an inert nonionic surfactant. Next, the insulin and glucagon receptors will be isolated, purified and characterized by CD and other physical tecniques. The complexes between these hormones and their receptors will also be studied in the presence and absence of phospholipids. The long-range objective of the proposed research is to understand the protein-lipid interactions and their structure-function relationship. In addition, the shape and conformation of myosin, its fragments and their complex formation with actin will continue to be investigated in order to understand the mechanism of muscle contraction.